Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a tetramer containing identical chains. It catalyzes the reversible oxidative phosphorylation of glyceraldehyde phosphate, which is an important step in energy production in carbohydrate metabolism. It binds to several proteins including actin, tubulin, amyloid precursors, polyglutamine peptides, DRPLA (dentorubral pallidoluic atrophy) and Huntington.
Phosphorylated GAPDH binds to cytoskeleton elements and controls microtubule dynamics in early secretory pathways. Poly(ADP-ribose) polymerase-1 (PARP1) interacts with GAPDH antibody A00227-1 to mediate brain damage in the presence of oxidative/nitrosative stress.
GAPDH is part of OCA-S, a multicomponent OCT1 (octamer motif binding factor) coactivator complex involved in the S-phase-dependent transcription of histone H2B. This association is responsible for linking the H2B transcriptional machinery with cell cycle regulation and cell metabolism. GAPDH is also part of the functional GAIT (interferon-γ-activated translation inhibitor) mRNP (messenger ribonucleoprotein).
GAPDH expression is impaired during melanoma progression. GAPDH (glyceraldehyde-3-phosphate dehydrogenase) is a catalytic enzyme known to be involved in glycolysis. GAPDH exists as an identical tetramer of 37 kDa subunit and catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde-3-phosphate in the presence of NADPH.
In addition to playing a key role in glycolysis, GAPDH is ubiquitous and exhibits other activities unrelated to its glycolytic function. GAPDH has been reported to be involved in DNA replication, DNA repair, nuclear RNA export, membrane fusion, and microtubule attachment.
Studies suggest that GAPDH plays an important role in the expression of genes observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases. In addition, GAPDH is involved in other cellular processes ranging from membrane fusion to neuronal apoptosis in cancer.